1w0m: Difference between revisions

New page: left|200px<br /> <applet load="1w0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w0m, resolution 2.5Å" /> '''TRIOSEPHOSPHATE ISOM...
 
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'''TRIOSEPHOSPHATE ISOMERASE FROM THERMOPROTEUS TENAX'''<br />


==Overview==
==Triosephosphate isomerase from Thermoproteus tenax==
Triosephophate isomerase (TIM) is a dimeric enzyme in eucarya, bacteria, and mesophilic archaea. In hyperthermophilic archaea, however, TIM exists, as a tetramer composed of monomers that are about 10% shorter than other, eucaryal and bacterial TIM monomers. We report here the crystal structure, of TIM from Thermoproteus tenax, a hyperthermophilic archaeon that has an, optimum growth temperature of 86 degrees C. The structure was determined, from both a hexagonal and an orthorhombic crystal form to resolutions of, 2.5A and 2.3A, and refined to R-factors of 19.7% and 21.5%, respectively., In both crystal forms, T.tenax TIM exists as a tetramer of the familiar, (betaalpha)(8)-barrel. In solution, however, and unlike other, hyperthermophilic TIMs, the T.tenax enzyme exhibits an equilibrium ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15342242 (full description)]]
<StructureSection load='1w0m' size='340' side='right'caption='[[1w0m]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1w0m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0M FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0m OCA], [https://pdbe.org/1w0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0m RCSB], [https://www.ebi.ac.uk/pdbsum/1w0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPIS_THETK TPIS_THETK]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w0m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Triosephophate isomerase (TIM) is a dimeric enzyme in eucarya, bacteria and mesophilic archaea. In hyperthermophilic archaea, however, TIM exists as a tetramer composed of monomers that are about 10% shorter than other eucaryal and bacterial TIM monomers. We report here the crystal structure of TIM from Thermoproteus tenax, a hyperthermophilic archaeon that has an optimum growth temperature of 86 degrees C. The structure was determined from both a hexagonal and an orthorhombic crystal form to resolutions of 2.5A and 2.3A, and refined to R-factors of 19.7% and 21.5%, respectively. In both crystal forms, T.tenax TIM exists as a tetramer of the familiar (betaalpha)(8)-barrel. In solution, however, and unlike other hyperthermophilic TIMs, the T.tenax enzyme exhibits an equilibrium between inactive dimers and active tetramers, which is shifted to the tetramer state through a specific interaction with glycerol-1-phosphate dehydrogenase of T.tenax. This observation is interpreted in physiological terms as a need to reduce the build-up of thermolabile metabolic intermediates that would be susceptible to destruction by heat. A detailed structural comparison with TIMs from organisms with growth optima ranging from 15 degrees C to 100 degrees C emphasizes the importance in hyperthermophilic proteins of the specific location of ionic interactions for thermal stability rather than their numbers, and shows a clear correlation between the reduction of heat-labile, surface-exposed Asn and Gln residues with thermoadaptation. The comparison confirms the increase in charged surface-exposed residues at the expense of polar residues.


==About this Structure==
Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature.,Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, Schramm A, Knura T, Stubbe K, Tjaden B, Hensel R J Mol Biol. 2004 Sep 17;342(3):861-75. PMID:15342242<ref>PMID:15342242</ref>
1W0M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W0M OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature., Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, Schramm A, Knura T, Stubbe K, Tjaden B, Hensel R, J Mol Biol. 2004 Sep 17;342(3):861-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15342242 15342242]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1w0m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoproteus tenax]]
[[Category: Thermoproteus tenax]]
[[Category: Hensel, R.]]
[[Category: Hensel R]]
[[Category: Knura, T.]]
[[Category: Knura T]]
[[Category: Lilie, H.]]
[[Category: Lilie H]]
[[Category: Lorentzen, E.]]
[[Category: Lorentzen E]]
[[Category: Pohl, E.]]
[[Category: Pohl E]]
[[Category: Schramm, A.]]
[[Category: Schramm A]]
[[Category: Stubbe, K.]]
[[Category: Stubbe K]]
[[Category: Taylor, G.]]
[[Category: Taylor G]]
[[Category: Tjaden, B.]]
[[Category: Tjaden B]]
[[Category: Walden, H.]]
[[Category: Walden H]]
[[Category: PO4]]
[[Category: gluconeogenesis]]
[[Category: glycolysis]]
[[Category: triosephosphate isomerase]]
 
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